Catalase-peroxidase - Streptomyces reticuli

Preferred order of sections

Names and origin

Protein names

Recommended name:
Catalase-peroxidase
Short name=CP
EC=1.11.1.21

Alternative name(s):
Peroxidase/catalase

Gene names

Name:	katG
Synonyms:	cpeB

Organism

Streptomyces reticuli

Taxonomic identifier

1926 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	740 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Ref.1
Catalytic activity	Donor + H₂O₂ = oxidized donor + 2 H₂O. HAMAP MF_01961 2 H₂O₂ = O₂ + 2 H₂O. HAMAP MF_01961
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per dimer. Ref.1
Subunit structure	Homodimer. Ref.1
Post-translational modification	The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme By similarity. HAMAP MF_01961
Sequence similarities	Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	catalase activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 740

740

Catalase-peroxidase HAMAP MF_01961

PRO_0000055577

Sites

Active site

109

1

Proton acceptor By similarity

Metal binding

272

1

Iron (heme axial ligand) By similarity

Site

105

1

Transition state stabilizer By similarity

Amino acid modifications

Cross-link

108 ↔ 231

Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-257) By similarity

Cross-link

231 ↔ 257

Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-108) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O87864 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: E21860AFE4B4A40E
Show »

FASTA

740

81,346

        10         20         30         40         50         60 
MTENHDAIVT DAKSEGSGGC PVAHDRALHP TQGGGNRQWW PERLNLKILA KNPAVANPLD 

        70         80         90        100        110        120 
EDFDYAEAFK ALDLAAVKRD IAEVLTTSQD WWPADFGNYG PLMIRMAWHS AGTYRISDGR 

       130        140        150        160        170        180 
GGAGAGQQRF APLNSWPDNG NLDKARRLLW PVKKKYGQSI SWADLLILTG NVALETMGFK 

       190        200        210        220        230        240 
TFGFGGGRAD VWEAEEDVYW GPETTWLDDR RYTGDRELEN PLGAVQMGLI YVNPEGPNGN 

       250        260        270        280        290        300 
PDPIAAARDI RETFRRMAMN DEETVALIAG GHTFGKTHGA GPADHVGADP EAASLEEQGL 

       310        320        330        340        350        360 
GWRSTYGTGK GADAITSGLE VTWTSTPTQW SNGFFKNLFE YEYELEQSPA GAHQWVAKNA 

       370        380        390        400        410        420 
PEIIPDAHDP SKKHRPRMLT TDLSLRFDPI YEPISRRFYE NPEEFADAFA RAWYKLTHRD 

       430        440        450        460        470        480 
MGPKSLYLGP EVPEETLLWQ DPLPEREGEL IDDADIAILK TKLLESGLSV SQLVTTAWAS 

       490        500        510        520        530        540 
ASTFRASDKR GGANGARIRL APQRGWEVND PDQLAQVLRT LENVQQEFNA SSGAKKVSLA 

       550        560        570        580        590        600 
DLIVLGGAAG VEKAAKEAGF EIQVPFTPGR VDATEEHTDV ESFEALEPTA DGFRNYLGKG 

       610        620        630        640        650        660 
NRLPAEYLLL DKANLLNLSA PEMTVLVGGL RVLGANHQQS QLGVFTKTPG VLTNDFFVNL 

       670        680        690        700        710        720 
LDMGTTWKAT SEDQTTFEGR DAATGEVKWA GSRADLVFGS NSELRALAEV YASDDAKEKF 

       730        740 
VKDFVAAWHK VMDADRFDLV

« Hide

References

[1]	"The mycelium-associated Streptomyces reticuli catalase-peroxidase, its gene and regulation by FurS." Zou P., Borovok I., Ortiz de Orue Lucana D., Muller D., Schrempf H. Microbiology 145:549-559(1999) [PubMed: 10217488] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT, HEME-BINDING. Strain: Tu45.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y14317 Genomic DNA. Translation: CAA74698.1.
3D structure databases
ProteinModelPortal	O87864.
SMR	O87864. Positions 33-739.
ModBase	Search...
Protein family/group databases
PeroxiBase	2330. SretCP01.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
HAMAP	MF_01961. Catal-peroxid. [Tree]
InterPro	IPR000763. Catalase_peroxidase. IPR010255. Haem_peroxidase. IPR002016. Haem_peroxidase_pln/fun/bac. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view]
Pfam	PF00141. peroxidase. 2 hits. [Graphical view]
PRINTS	PR00460. BPEROXIDASE. PR00458. PEROXIDASE.
SUPFAM	SSF48113. Peroxidase_super. 2 hits.
TIGRFAMs	TIGR00198. Cat_per_HPI. 1 hit.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KATG_STRRE

Accession

Primary (citable) accession number: O87864

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1998
Last modified:	October 19, 2011
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families